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{
"metadata": {
"accession": "PS51841",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR001322",
"hierarchy": null,
"name": {
"name": "Lamin-tail (LTD) domain profile",
"short": "LTD"
},
"description": [
{
"text": "<p>Intermediate filaments (IFs) constitute a major structural element of metazoan\ncells. They build two distinct systems: one inside the nucleus attached to the\ninner membrane, and one that is cytoplasmic, which connects intercellular\njunctional complexes situated at the plasma membrane with the outer nuclear\nmembrane. In both cases, their major function is assumed to be that of a\nmechanical stress absorber and an integrating device for the entire\ncytoskeleton. In the nucleus, the IF system is assembled from lamins, which\ntogether with an ever increasing number of associated transmembrane and\nchromatin-binding proteins constitute the nuclear lamina. Despite the large\ndiversity among IF proteins, they all share a similar structural building\nplan, with a long central alpha-helical 'rod' domain that is\nflanked by non-alpha-helical N- and C-terminal end domains called 'head' and\n'tail', respectively. Lamins exhibit a highly conserved globular C-terminal\nlamin-tail domain (LTD) which has the immunoglobulin (Ig) fold. Invertebrate cytoplasmic IFs share sequence similarity with\nnuclear lamins and also contain a C-terminal tail domain with homology to the\nLTD [[cite:PUB00088683]][[cite:PUB00057231]][[cite:PUB00088684]].\n\nDomains homologous to the LTD have been detected in several uncharacterized\nproteins from phylogenetically diverse bacteria and two archaea,\nMethanosarcina and Halobacterium. In several bacterial proteins, the LTD\ncooccurs with membrane-associated hydrolases of the metallo-beta-lactamase,\nsynaptojanin, and calcineurin-like phosphoesterase superfamilies. In other\nsecreted or periplasmic bacterial proteins, the LTDs are associated with\noligosaccharide-binding domains or are present as multiple tandem repeats in a\nsingle protein. These associations suggest a potential role for the\nprokaryotic LTDs in tethering proteins to the membrane or membrane-associated\nstructures. In contrast to the bacterial homologs, all animal LTDs are closely\nrelated and are contained in proteins with a stereotypic architecture. The\nprecursor of the animal LTD might have been acquired via horizontal gene\ntransfer from bacteria relatively late in the evolution of the eukaryotic\ncrown group. Subsequent to this acquisition, a coiled-coil domain, derived\nfrom preexisting intermediate filament coil-coils, might have been fused to\nthe N-termini of the LTD [[cite:PUB00057231]].\n\nThe LTD domain could be involved both in protein and DNA binding [[cite:PUB00026148]].\n\nTh LTD domain adopts an Ig-like fold of type s. It consists\nof a 2-layered sandwich of 9 anti-parallel beta-strands arranged in two beta-\nsheets with a Greek key topology. One of the sheets has five beta-strands\nwhile the other has four. Seven of the 9 strands are present in the classical\nIg fold topology [[cite:PUB00026148]][[cite:PUB00088685]].\n\nSome proteins known to contain a LTD domain are listed below:\n\n - Animal nuclear lamins, together with lamin-associated proteins, maintain\n nuclear shape and provide a structural support for chromosomes and\n replicating DNA.\n - Chloroflexus aurantiacus Chlo1887.\n - Caenorhabditis elegans intermediate filament protein ifc-2 [[cite:PUB00108428]].\n - Caenorhabditis elegans intermediate filament protein ifd-1.\n\nThe profile we developed covers the entire LTD domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00088685": {
"PMID": 22265972,
"ISBN": null,
"volume": "586",
"issue": "4",
"year": 2012,
"title": "Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1.",
"URL": null,
"raw_pages": "314-8",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Ruan J",
"Xu C",
"Bian C",
"Lam R",
"Wang JP",
"Kania J",
"Min J",
"Zang J."
],
"DOI_URL": "https://doi.org/10.1016/j.febslet.2012.01.007"
},
"PUB00088684": {
"PMID": 1794458,
"ISBN": null,
"volume": "19",
"issue": "4",
"year": 1991,
"title": "Aspects of the evolution of the lamin/intermediate filament protein family: a current analysis of invertebrate intermediate filament proteins.",
"URL": null,
"raw_pages": "1021-3",
"medline_journal": "Biochem Soc Trans",
"ISO_journal": "Biochem. Soc. Trans.",
"authors": [
"Weber K",
"Riemer D",
"Dodemont H."
],
"DOI_URL": "https://doi.org/10.1042/bst0191021"
},
"PUB00108428": {
"PMID": 18452552,
"ISBN": null,
"volume": "76",
"issue": "8",
"year": 2008,
"title": "Maintenance of the intestinal tube in Caenorhabditis elegans: the role of the intermediate filament protein IFC-2.",
"URL": null,
"raw_pages": "881-96",
"medline_journal": "Differentiation",
"ISO_journal": "Differentiation",
"authors": [
"Husken K",
"Wiesenfahrt T",
"Abraham C",
"Windoffer R",
"Bossinger O",
"Leube RE."
],
"DOI_URL": null
},
"PUB00057231": {
"PMID": 15611647,
"ISBN": null,
"volume": "3",
"issue": "12",
"year": 2004,
"title": "Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex.",
"URL": null,
"raw_pages": "1612-37",
"medline_journal": "Cell Cycle",
"ISO_journal": "Cell Cycle",
"authors": [
"Mans BJ",
"Anantharaman V",
"Aravind L",
"Koonin EV."
],
"DOI_URL": null
},
"PUB00088683": {
"PMID": 17551517,
"ISBN": null,
"volume": "8",
"issue": "7",
"year": 2007,
"title": "Intermediate filaments: from cell architecture to nanomechanics.",
"URL": null,
"raw_pages": "562-73",
"medline_journal": "Nat Rev Mol Cell Biol",
"ISO_journal": "Nat. Rev. Mol. Cell Biol.",
"authors": [
"Herrmann H",
"Bar H",
"Kreplak L",
"Strelkov SV",
"Aebi U."
],
"DOI_URL": "https://doi.org/10.1038/nrm2197"
},
"PUB00026148": {
"PMID": 12057196,
"ISBN": null,
"volume": "10",
"issue": "6",
"year": 2002,
"title": "The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy.",
"URL": null,
"raw_pages": "811-23",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Krimm I",
"Ostlund C",
"Gilquin B",
"Couprie J",
"Hossenlopp P",
"Mornon JP",
"Bonne G",
"Courvalin JC",
"Worman HJ",
"Zinn-Justin S."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(02)00777-3"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 27074,
"pathways": 0,
"proteins": 23709,
"proteomes": 7827,
"sets": 0,
"structural_models": {
"alphafold": 16979,
"bfvd": 0
},
"structures": 17,
"taxa": 16110
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3umn",
"name": "Crystal Structure of Lamin-B1"
}
}
}
